Folding and oligomerization properties of a soluble and secreted form of the paramyxovirus hemagglutinin-neuraminidase glycoprotein
Identifieur interne : 002088 ( Main/Exploration ); précédent : 002087; suivant : 002089Folding and oligomerization properties of a soluble and secreted form of the paramyxovirus hemagglutinin-neuraminidase glycoprotein
Auteurs : Griffith D. Parks [États-Unis] ; Robert A. Lamb [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1990.
English descriptors
- Teeft :
- Carbohydrate, Carbohydrate residues, Cdna, Cell biol, Cell lysates, Cell surface, Cells expressrng, Chase medium, Chase period, Cleavable signal sequence, Cytoplasmic tail, Digestion, Dimer, Dimeric, Dimeric form, Disulfide, Doms, Ectodomain, Endo, Endoplasmic reticulum, Equal portions, External domain, Extracellular, Gething, Glycoprotein, Hydrophobic domain, Immunoprecipitated, Influenza, Influenza virus, Influenza virus neuraminidase, Integral membrane protein, Integral membrane proteins, Intermolecular, Intracellular, Intracellular transport, Lamb, Membrane, Molecule, Monoclonal antibodies, Monomer, Monomeric, Monomeric form, Native conformation, Neuraminidase, Neuraminidase activity, Nonreducing, Nonreducing conditions, Oligomeric, Oligomeric form, Oligomerization, Paramyxovirus, Paterson, Pellet fraction, Polyclonal, Polypeptide, Radiolabeled, Recombinant, Sedimentation, Sendai virus, Signal peptidase, Signal sequence, Small amount, Small amounts, Soluble, Soluble form, Soluble forms, Soluble proteins, Sucrose, Sucrose gradient sedimentation, Sucrose gradients, Tetramers, Vast majority, Viral.
Abstract
Abstract: The paramyxovirus SV5 hemagglutinin-neuraminidase (HN) glycoprotein (a type II integral membrane protein) was converted into a soluble and secreted form (HN-F) by replacing the HN signal/anchor domain with a hydrophobic domain that can act as a cleavable signal sequence. Approximately 40% of the HN-F synthesized was secreted from cells (t case1 2 ∼ 2.5−3 hr). The extracellular HN-F molecules were identified as disulfide-linked dimers and the majority of the population of molecules were resistant to endoglycosidase H digestion. Examination of the oligomeric form of the secreted HN-F, by sucrose density gradient sedimentation, indicated that under conditions where HN was a tetramer, HN-F was found to be a dimer, and no extracellular HN-F monomeric species could be detected. Secreted HN-F was fully reactive with conformation-specific monoclonal antibodies and was enzymatically active as shown by HN-F having neuraminidase activity. Examination of the intracellular HN-F species indicated that HN-F monomers were slowly converted to the disulfide-linked form and that under the sucrose density gradient sedimentation conditions used the HNF monomers aggregated. Some of the HN-F monomers were degraded intracellularly. These data are discussed in relationship to the seemingly different folding and oligomerization requirements for the intracellular transport of soluble and membrane bound forms of a glycoprotein. The soluble and biologically active form of HN may be suitable for further structural and enzymatic studies.
Url:
DOI: 10.1016/0042-6822(90)90347-T
Affiliations:
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Lamb</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500</wicri:regionArea><wicri:noRegion>Illinois 60208-3500</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990">1990</date><biblScope unit="volume">178</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="498">498</biblScope><biblScope unit="page" to="508">508</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Carbohydrate</term><term>Carbohydrate residues</term><term>Cdna</term><term>Cell biol</term><term>Cell lysates</term><term>Cell surface</term><term>Cells expressrng</term><term>Chase medium</term><term>Chase period</term><term>Cleavable signal sequence</term><term>Cytoplasmic tail</term><term>Digestion</term><term>Dimer</term><term>Dimeric</term><term>Dimeric form</term><term>Disulfide</term><term>Doms</term><term>Ectodomain</term><term>Endo</term><term>Endoplasmic reticulum</term><term>Equal portions</term><term>External domain</term><term>Extracellular</term><term>Gething</term><term>Glycoprotein</term><term>Hydrophobic domain</term><term>Immunoprecipitated</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Integral membrane protein</term><term>Integral membrane proteins</term><term>Intermolecular</term><term>Intracellular</term><term>Intracellular transport</term><term>Lamb</term><term>Membrane</term><term>Molecule</term><term>Monoclonal antibodies</term><term>Monomer</term><term>Monomeric</term><term>Monomeric form</term><term>Native conformation</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Nonreducing</term><term>Nonreducing conditions</term><term>Oligomeric</term><term>Oligomeric form</term><term>Oligomerization</term><term>Paramyxovirus</term><term>Paterson</term><term>Pellet fraction</term><term>Polyclonal</term><term>Polypeptide</term><term>Radiolabeled</term><term>Recombinant</term><term>Sedimentation</term><term>Sendai virus</term><term>Signal peptidase</term><term>Signal sequence</term><term>Small amount</term><term>Small amounts</term><term>Soluble</term><term>Soluble form</term><term>Soluble forms</term><term>Soluble proteins</term><term>Sucrose</term><term>Sucrose gradient sedimentation</term><term>Sucrose gradients</term><term>Tetramers</term><term>Vast majority</term><term>Viral</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The paramyxovirus SV5 hemagglutinin-neuraminidase (HN) glycoprotein (a type II integral membrane protein) was converted into a soluble and secreted form (HN-F) by replacing the HN signal/anchor domain with a hydrophobic domain that can act as a cleavable signal sequence. Approximately 40% of the HN-F synthesized was secreted from cells (t case1 2 ∼ 2.5−3 hr). The extracellular HN-F molecules were identified as disulfide-linked dimers and the majority of the population of molecules were resistant to endoglycosidase H digestion. Examination of the oligomeric form of the secreted HN-F, by sucrose density gradient sedimentation, indicated that under conditions where HN was a tetramer, HN-F was found to be a dimer, and no extracellular HN-F monomeric species could be detected. Secreted HN-F was fully reactive with conformation-specific monoclonal antibodies and was enzymatically active as shown by HN-F having neuraminidase activity. Examination of the intracellular HN-F species indicated that HN-F monomers were slowly converted to the disulfide-linked form and that under the sucrose density gradient sedimentation conditions used the HNF monomers aggregated. Some of the HN-F monomers were degraded intracellularly. These data are discussed in relationship to the seemingly different folding and oligomerization requirements for the intracellular transport of soluble and membrane bound forms of a glycoprotein. The soluble and biologically active form of HN may be suitable for further structural and enzymatic studies.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Parks, Griffith D" sort="Parks, Griffith D" uniqKey="Parks G" first="Griffith D" last="Parks">Griffith D. Parks</name></noRegion><name sortKey="Lamb, Robert A" sort="Lamb, Robert A" uniqKey="Lamb R" first="Robert A" last="Lamb">Robert A. Lamb</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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